BMRB Entry 36097

Title:
Structure of FLN IG21 domain in complex with C-terminal peptide of beta-2
Deposition date:
2017-06-07
Original release date:
2018-06-18
Authors:
Chatterjee, D.; Lu, L.; Bhattacharjya, S.
Citation:

Citation: Chatterjee, D.; Lu, L.; Bhattachrjya, S.. "Structure of FLN IG21 domain in complex with C-terminal peptide of beta-2"  .

Assembly members:

Assembly members:
FLN IG21 domain, polymer, 116 residues, 11716.865 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: BAC cloning vector attB-P[acman]-ApR-F-2-5-attB

Data sets:
Data typeCount
13C chemical shifts159
15N chemical shifts87
1H chemical shifts361

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 116 residues - 11716.865 Da.

1   PROLEUPHELYSSERALATHRTHRTHRVAL
2   METASNGLYALASERGLYSERGLYALASER
3   GLYSERGLYGLYALAHISLYSVALARGALA
4   GLYGLYPROGLYLEUGLUARGALAGLUALA
5   GLYVALPROALAGLUPHESERILETRPTHR
6   ARGGLUALAGLYALAGLYGLYLEUALAILE
7   ALAVALGLUGLYPROSERLYSALAGLUILE
8   SERPHEGLUASPARGLYSASPGLYSERCYS
9   GLYVALALATYRVALVALGLNGLUPROGLY
10   ASPTYRGLUVALSERVALLYSPHEASNGLU
11   GLUHISILEPROASPSERPROPHEVALVAL
12   PROVALALASERPROSER

Samples:

sample_1: FLN IG21 domain, [U-13C; U-15N], 300 uM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks